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( General CGTase assay (iodine method).The activity of CGTase was assayed using amylose AS-30 as a substrate by measuring the decrease in iodine- staining CGTase activity and β-cyclodextrin production were determined by phenolphthalein assay method described by Goel and Nene [15] with minor modification. Isolate showing highest CGTase activity was characterized morphologically and biochemically. CD was produced using CGTase which was further used for drug 12 Nov 2019 lans CGTase mutant revealed that this salt bridge is also formed in the mutant. Thus, the activity half-life of this enzyme can be enhanced by The enzyme variant is obtainable by modifying a CGTase or a maltogenic glycosyltransferase (CGTase) polypeptides with modified hydrolysis activity 8 Jun 2017 β-CGTase is one of the important α-amylase family, and CGTase is the first enzyme of all the transglycosylases. In general, the cyclization activity The CGTase activity was measured as β-cyclodextrin. (β-CD) forming activity by the PHP method [33]. Fifty- microliters crude enzyme were added to 1 ml of 2%.
In general, the cyclization activity The CGTase activity was measured as β-cyclodextrin. (β-CD) forming activity by the PHP method [33]. Fifty- microliters crude enzyme were added to 1 ml of 2%. yeast extract, peptone and starch showed highest impact on the CGTase production. CGTase activity was measured by decrease of phenolphthalein colour. nitrogen source for CGTase production. Ca2+ influences the CGTase production and Zn2+ inhibits the enzyme.
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Both enzymes also hydrolyzed α-, β-, and γ-cyclodextrin. Very interestingly, AmyA, but not AmyB, displayed high transglycosylation activity on maltooligosaccharides and also had significant β-cyclodextrin glycosyltransferase (CGTase) activity. CGTase activity has not been reported for typical α-amylases before.
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CGTase is an enzyme common to many bacterial species, in particular of the Bacillus genus (e.g. B. circulans, B. macerans and B. stearothermophilus) and Brevibacillus brevis. CGTase activity is inhibited by a high substrate concentration and by products formed during reaction,,,,. Therefore, this fact must be taken into account in order to improve the yield and selectivity for CD industrial production. Cyclodextrin glucanotransferases (CGTases; EC 2.4.1.19) have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization). γ-Cyclodextrin glycosyltransferase (γ-CGTase) catalyzes the biotransformation of low-cost starch into valuable γ-cyclodextrin (γ-CD), which is widely applied in biotechnology, food, and pharmaceutical industries. CGTase activity was assayed as described by Kato and Horikoshi [ 5 ].
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Bhargavi Kumaraswamy. 689 av J Wouters · 2005 · Citerat av 1 — cgt, CGTase, Differential display, Symbiosis, Nostoc, Gunnera and Gunnera sp.
in a conserved GGHGG loop and allows for comparable α-retaining and β-inverting activity in an
Beneficial Activity by Bacillus subtilis.
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Furthermore, Phe-183 and Phe-259 have specific roles in the transglycosylation reactions catalyzed by CGTase. CGTase activity was found in yeast extract supplemented medium and low in tryptophan supplementation. Maximum CGTase activity reached at 24 h of incubation in all media except medium supplemented with ammonium sulphate (Fig. 5).
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We discovered that CGTase has antimicrobial activity and induces resistance. In addition, we have revealed the key do-mains responsible for its hydrolytic activity and resistance induction. Further experiments demonstrated that CGTase is a potential func - Polyethylene glycol-6000 showed a 26 % increase in the CGTase activity. The kinetic parameters Km and Vmax were 10 mg/ml and 146 µmol/mg min, respectively, for purified CGTase. CGTase can catalyse four reactions: cyclization, coupling, disproportionation, and hydrolysis (Li et al., 2014b), though the hydrolysis activity is relatively weak (Costa et al., 2009). CGTase is a member of glycoside hydrolase family 13 (GH13) (Buchholz & Seibel, 2008 ; Stam et al., 2006 ).
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23 Aug 2017 When expression was induced at 25 °C for 32 h, and then the temperature was shifted to 30 °C, the extracellular α-CGTase activity at 90 h was 45 Catalytic activities[edit].
23 Aug 2017 When expression was induced at 25 °C for 32 h, and then the temperature was shifted to 30 °C, the extracellular α-CGTase activity at 90 h was 45 Catalytic activities[edit]. All of the CGTases can catalyze up to four reactions: cyclization, coupling, disproportionation and hydrolysis. All these activities share the 23 Sep 2016 megaterium in a submerged fermentation. Afterwards, the CGTase was purified partially and its activity to synthesize α-, β-, and γ-CDs was It was reported that CGTases are active on both starch fractions: amylose and amylopectin but the high amylopectin content were preferred for CGTase activity. ( General CGTase assay (iodine method).The activity of CGTase was assayed using amylose AS-30 as a substrate by measuring the decrease in iodine- staining CGTase activity and β-cyclodextrin production were determined by phenolphthalein assay method described by Goel and Nene [15] with minor modification.